Two N-Terminal Domains of Kv4 K + Channels Regulate Binding to and Modulation by KChIP1
The family of calcium binding proteins called KChIPs associates with Kv4 family K + channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7–11 a...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 2004-02, Vol.41 (4), p.587-598 |
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| creator | Scannevin, Robert H Wang, KeWei Jow, Flora Megules, Jennifer Kopsco, David C Edris, Wade Carroll, Karen C Lü, Qiang Xu, Weixin Xu, Zhangbao Katz, Alan H Olland, Stephane Lin, Laura Taylor, Meggin Stahl, Mark Malakian, Karl Somers, Will Mosyak, Lydia Bowlby, Mark R Chanda, Pranab Rhodes, Kenneth J |
| description | The family of calcium binding proteins called KChIPs associates with Kv4 family K
+ channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7–11 and 71–90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71–90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71–90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits. |
| doi_str_mv | 10.1016/S0896-6273(04)00049-2 |
| format | Article |
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+ channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7–11 and 71–90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71–90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71–90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits.</description><identifier>ISSN: 0896-6273</identifier><identifier>EISSN: 1097-4199</identifier><identifier>DOI: 10.1016/S0896-6273(04)00049-2</identifier><identifier>PMID: 14980207</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence - physiology ; Amino acids ; Animals ; Binding sites ; Binding Sites - genetics ; Calcium-Binding Proteins - chemistry ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Cell Line ; Cell Membrane - chemistry ; Cell Membrane - genetics ; Cell Membrane - metabolism ; Crystal structure ; Crystallography, X-Ray ; Humans ; Kv Channel-Interacting Proteins ; Medical research ; Membrane Potentials - genetics ; Models, Molecular ; Mutagenesis, Site-Directed - genetics ; Mutation ; Oocytes - metabolism ; Patch-Clamp Techniques ; Potassium Channels - chemistry ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated ; Protein Binding - genetics ; Protein Structure, Tertiary - genetics ; Protein Subunits ; Proteins ; Shal Potassium Channels</subject><ispartof>Neuron (Cambridge, Mass.), 2004-02, Vol.41 (4), p.587-598</ispartof><rights>2004 Cell Press</rights><rights>Copyright Elsevier Limited Feb 19, 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-9b80b0fe862e6fd5d430f57d5a9e0951116bc62420046683ba0839c6692646533</citedby><cites>FETCH-LOGICAL-c556t-9b80b0fe862e6fd5d430f57d5a9e0951116bc62420046683ba0839c6692646533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0896627304000492$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14980207$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scannevin, Robert H</creatorcontrib><creatorcontrib>Wang, KeWei</creatorcontrib><creatorcontrib>Jow, Flora</creatorcontrib><creatorcontrib>Megules, Jennifer</creatorcontrib><creatorcontrib>Kopsco, David C</creatorcontrib><creatorcontrib>Edris, Wade</creatorcontrib><creatorcontrib>Carroll, Karen C</creatorcontrib><creatorcontrib>Lü, Qiang</creatorcontrib><creatorcontrib>Xu, Weixin</creatorcontrib><creatorcontrib>Xu, Zhangbao</creatorcontrib><creatorcontrib>Katz, Alan H</creatorcontrib><creatorcontrib>Olland, Stephane</creatorcontrib><creatorcontrib>Lin, Laura</creatorcontrib><creatorcontrib>Taylor, Meggin</creatorcontrib><creatorcontrib>Stahl, Mark</creatorcontrib><creatorcontrib>Malakian, Karl</creatorcontrib><creatorcontrib>Somers, Will</creatorcontrib><creatorcontrib>Mosyak, Lydia</creatorcontrib><creatorcontrib>Bowlby, Mark R</creatorcontrib><creatorcontrib>Chanda, Pranab</creatorcontrib><creatorcontrib>Rhodes, Kenneth J</creatorcontrib><title>Two N-Terminal Domains of Kv4 K + Channels Regulate Binding to and Modulation by KChIP1</title><title>Neuron (Cambridge, Mass.)</title><addtitle>Neuron</addtitle><description>The family of calcium binding proteins called KChIPs associates with Kv4 family K
+ channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7–11 and 71–90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71–90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71–90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits.</description><subject>Amino Acid Sequence - physiology</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Binding Sites - genetics</subject><subject>Calcium-Binding Proteins - chemistry</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane - metabolism</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Humans</subject><subject>Kv Channel-Interacting Proteins</subject><subject>Medical research</subject><subject>Membrane Potentials - genetics</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed - genetics</subject><subject>Mutation</subject><subject>Oocytes - metabolism</subject><subject>Patch-Clamp Techniques</subject><subject>Potassium Channels - chemistry</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - metabolism</subject><subject>Potassium Channels, Voltage-Gated</subject><subject>Protein Binding - genetics</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Protein Subunits</subject><subject>Proteins</subject><subject>Shal Potassium Channels</subject><issn>0896-6273</issn><issn>1097-4199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMoWqs_QQl4UWR1kk3SzUm0ftL6gVY8huwmq5E20WSr-O_d2qJHTwPD877DPAhtETggQMThAxRSZIL28l1gewDAZEaXUIeA7GWMSLmMOr_IGlpP6RWAMC7JKlojTBZAoddBT6PPgG-ykY0T5_UYn4aJdj7hUOPBB8MDvI_7L9p7O0743j5Px7qx-MR54_wzbgLW3uDrYGZ7Fzwuv_Cg_3J1RzbQSq3HyW4uZhc9np-N-pfZ8Pbiqn88zCrORZPJsoASalsIakVtuGE51LxnuJYWJCeEiLISlNH2PyGKvNRQ5LISQlLBBM_zLtqZ977F8D61qVGvYRrbT5IiHHJBW7RoKT6nqhhSirZWb9FNdPxSBNRMp_rRqWauFDD1o1PRNre9aJ-WE2v-Ugt_LXA0B1o_9sPZqFLlrK-scdFWjTLB_XPiGxeygEg</recordid><startdate>20040219</startdate><enddate>20040219</enddate><creator>Scannevin, Robert H</creator><creator>Wang, KeWei</creator><creator>Jow, Flora</creator><creator>Megules, Jennifer</creator><creator>Kopsco, David C</creator><creator>Edris, Wade</creator><creator>Carroll, Karen C</creator><creator>Lü, Qiang</creator><creator>Xu, Weixin</creator><creator>Xu, Zhangbao</creator><creator>Katz, Alan H</creator><creator>Olland, Stephane</creator><creator>Lin, Laura</creator><creator>Taylor, Meggin</creator><creator>Stahl, Mark</creator><creator>Malakian, Karl</creator><creator>Somers, Will</creator><creator>Mosyak, Lydia</creator><creator>Bowlby, Mark R</creator><creator>Chanda, Pranab</creator><creator>Rhodes, Kenneth J</creator><general>Elsevier Inc</general><general>Elsevier Limited</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20040219</creationdate><title>Two N-Terminal Domains of Kv4 K + Channels Regulate Binding to and Modulation by KChIP1</title><author>Scannevin, Robert H ; Wang, KeWei ; Jow, Flora ; Megules, Jennifer ; Kopsco, David C ; Edris, Wade ; Carroll, Karen C ; Lü, Qiang ; Xu, Weixin ; Xu, Zhangbao ; Katz, Alan H ; Olland, Stephane ; Lin, Laura ; Taylor, Meggin ; Stahl, Mark ; Malakian, Karl ; Somers, Will ; Mosyak, Lydia ; Bowlby, Mark R ; Chanda, Pranab ; Rhodes, Kenneth J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-9b80b0fe862e6fd5d430f57d5a9e0951116bc62420046683ba0839c6692646533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence - physiology</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Binding Sites - genetics</topic><topic>Calcium-Binding Proteins - chemistry</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - genetics</topic><topic>Cell Membrane - metabolism</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Humans</topic><topic>Kv Channel-Interacting Proteins</topic><topic>Medical research</topic><topic>Membrane Potentials - genetics</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed - genetics</topic><topic>Mutation</topic><topic>Oocytes - metabolism</topic><topic>Patch-Clamp Techniques</topic><topic>Potassium Channels - chemistry</topic><topic>Potassium Channels - genetics</topic><topic>Potassium Channels - metabolism</topic><topic>Potassium Channels, Voltage-Gated</topic><topic>Protein Binding - genetics</topic><topic>Protein Structure, Tertiary - genetics</topic><topic>Protein Subunits</topic><topic>Proteins</topic><topic>Shal Potassium Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scannevin, Robert H</creatorcontrib><creatorcontrib>Wang, KeWei</creatorcontrib><creatorcontrib>Jow, Flora</creatorcontrib><creatorcontrib>Megules, Jennifer</creatorcontrib><creatorcontrib>Kopsco, David C</creatorcontrib><creatorcontrib>Edris, Wade</creatorcontrib><creatorcontrib>Carroll, Karen C</creatorcontrib><creatorcontrib>Lü, Qiang</creatorcontrib><creatorcontrib>Xu, Weixin</creatorcontrib><creatorcontrib>Xu, Zhangbao</creatorcontrib><creatorcontrib>Katz, Alan H</creatorcontrib><creatorcontrib>Olland, Stephane</creatorcontrib><creatorcontrib>Lin, Laura</creatorcontrib><creatorcontrib>Taylor, Meggin</creatorcontrib><creatorcontrib>Stahl, Mark</creatorcontrib><creatorcontrib>Malakian, Karl</creatorcontrib><creatorcontrib>Somers, Will</creatorcontrib><creatorcontrib>Mosyak, Lydia</creatorcontrib><creatorcontrib>Bowlby, Mark R</creatorcontrib><creatorcontrib>Chanda, Pranab</creatorcontrib><creatorcontrib>Rhodes, Kenneth J</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Neuron (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scannevin, Robert H</au><au>Wang, KeWei</au><au>Jow, Flora</au><au>Megules, Jennifer</au><au>Kopsco, David C</au><au>Edris, Wade</au><au>Carroll, Karen C</au><au>Lü, Qiang</au><au>Xu, Weixin</au><au>Xu, Zhangbao</au><au>Katz, Alan H</au><au>Olland, Stephane</au><au>Lin, Laura</au><au>Taylor, Meggin</au><au>Stahl, Mark</au><au>Malakian, Karl</au><au>Somers, Will</au><au>Mosyak, Lydia</au><au>Bowlby, Mark R</au><au>Chanda, Pranab</au><au>Rhodes, Kenneth J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two N-Terminal Domains of Kv4 K + Channels Regulate Binding to and Modulation by KChIP1</atitle><jtitle>Neuron (Cambridge, Mass.)</jtitle><addtitle>Neuron</addtitle><date>2004-02-19</date><risdate>2004</risdate><volume>41</volume><issue>4</issue><spage>587</spage><epage>598</epage><pages>587-598</pages><issn>0896-6273</issn><eissn>1097-4199</eissn><abstract>The family of calcium binding proteins called KChIPs associates with Kv4 family K
+ channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7–11 and 71–90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71–90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71–90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14980207</pmid><doi>10.1016/S0896-6273(04)00049-2</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence - physiology Amino acids Animals Binding sites Binding Sites - genetics Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cell Line Cell Membrane - chemistry Cell Membrane - genetics Cell Membrane - metabolism Crystal structure Crystallography, X-Ray Humans Kv Channel-Interacting Proteins Medical research Membrane Potentials - genetics Models, Molecular Mutagenesis, Site-Directed - genetics Mutation Oocytes - metabolism Patch-Clamp Techniques Potassium Channels - chemistry Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated Protein Binding - genetics Protein Structure, Tertiary - genetics Protein Subunits Proteins Shal Potassium Channels |
| title | Two N-Terminal Domains of Kv4 K + Channels Regulate Binding to and Modulation by KChIP1 |
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